Hostname: page-component-cd9895bd7-gvvz8 Total loading time: 0 Render date: 2024-12-25T02:16:15.128Z Has data issue: false hasContentIssue false
  • English
  • Français

Characteristics of skeletal muscle growth and protein turnover in a fast-growing rat strain

Published online by Cambridge University Press:  09 March 2007

P. C. Bates  and
D. J. Millward
P. C. Bates
Affiliation:
Clinical Nutrition and Metabolism Unit, Department of Human Nutrition, London School of Hygiene and Tropical Medicine, 4 St Pancras Way, London NW1 2PE
D. J. Millward
Affiliation:
Clinical Nutrition and Metabolism Unit, Department of Human Nutrition, London School of Hygiene and Tropical Medicine, 4 St Pancras Way, London NW1 2PE
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

1. Protein turnover and muscle composition has been studied in rat skeletal muscle throughout development in a relatively-fast-growing rat strain.

2. Muscle growth involved an increase in the total DNA and in the DNA-unit size as indicated by protein: DNA. As a result of the latter increase together with no change in RNA: DNA, the RNA concentration fell throughout development.

3. Rates of protein synthesis measured in vivo by the continuous intravenous infusion method fell throughout development from 15.6%/d at 25 d to 4.46%/d at 320 d, and these changes reflected mainly the fall in RNA concentration, since there was no marked change in the rate of protein synthesis per unit RNA.

4. The rate of protein degradation, measured as the difference between rates of protein synthesis and growth, fell from 9.82%/d at 25 d to 4.46%/d at 320 d.

5. When these changes in protein turnover throughout development are compared with measurements made previously in a slow-growing strain it would appear that the faster growth was achieved as a result of increased efficiency of protein synthesis (defined as net synthesis: over-all synthesis) and this occurred mainly because of lower rate of protein degradation.

Type
Papers of direct relevance to Clinical and Human Nutrition
Information
British Journal of Nutrition , Volume 46 , Issue 1 , July 1981 , pp. 7 - 13
Copyright
Copyright © The Nutrition Society 1981

References

REFERENCES

Bates, P. C., De Coster, T., Grimble, G. K., Holloszy, J. O., Millward, D. J. & Rennie, M. J. (1980). J. Physiol., Lond. 299, 52P.Google Scholar
Bates, P. C. & Millward, D. J. (1978). Proc. Nutr. Soc. 37, 19A.Google Scholar
Brown, J. G. & Millward, D. L. (1980). Biochem. Soc. Trans. 8, 366.CrossRefGoogle Scholar
Brown, J. G. & Millward, D. J. (1981). Biochem. J. (In the Press).Google Scholar
Laurent, G. J. & Millward, D. J. (1980). Fedn Proc. Fedn Am. Socs exp. Biol. 39, 42.Google Scholar
Laurent, G. J., Sparrow, M. P. & Millward, D. J. (1978). Biochem. J. 176, 407.CrossRefGoogle Scholar
Maruyama, K., Sunde, M. L. & Swick, R. W. (1978). Biochem. J. 176, 573.CrossRefGoogle Scholar
Millward, D. J. (1978). Biochem. Soc. Trans. 6, 494.CrossRefGoogle Scholar
Millward, D. J. (1980 a). In Degradative Processes in Heart and Skeletal Muscle, pp. 161–199. [Wildenthal, K. editor]. Amsterdam: North Holland.Google Scholar
Millward, D. J. (1980 b). In Comprehensive Biochemistry, vol. 19b, pp. 153–232 [Neuberger, A. editor]. Amsterdam: Elsevier North-Holland.Google Scholar
Millward, D. J., Bates, P. C., Brown, J. G., Rosochacki, S. R. & Rennie, M. J. (1980). Ciba Fdn Symp. no. 75 p. 307.Google Scholar
Millward, D. J., Bates, P. C. & Laurent, G. (1977). Proc. Nutr. Soc. 36, 35A.Google Scholar
Millward, D. J., Bates, P. C. & Rosochacki, S. R. (1981). Reproduction, Nutrition Development. (In the Press).Google Scholar
Millward, D. J., Garlick, P. J., James, W. P. T., Nnanyelugo, D. O. & Ryatt, J. S. (1973). Nature, Lond. 241, 204.CrossRefGoogle Scholar
Millward, D. J., Garlick, P. J., Nnanyelugo, D. O. & Waterlow, J. C. (1976). Biochem. J. 156, 185.CrossRefGoogle Scholar
Millward, D. J., Garlick, P. J. & Reeds, P. J. (1976). Proc. Nutr. Soc. 35, 339.CrossRefGoogle Scholar
Millward, D. J., Garlick, P. J., Stewart, R. J. C., Nnanyelugo, D. O. & Waterlow, J. C. (1975). Biochem. J. 150, 235.CrossRefGoogle Scholar
Millward, D. J., Nnanyelugo, D. O., James, W. P. T. & Garlick, P. J. (1974). Br. J. Nutr. 32, 127.CrossRefGoogle Scholar
Millward, D. J. & Waterlow, J. C. (1978). Fedn Proc. Fedn Am. Socs exp. Biol. 37, 2283.Google Scholar
Ross, M. H., Lustbader, E. & Bras, G. (1976). Nature, Lond. 262, 548.CrossRefGoogle Scholar
Vernon, B. G. & Buttery, P. J. (1976). Br. J. Nutr. 36, 575.CrossRefGoogle Scholar
Walker, D. M. & Norton, B. W. (1970). Publ. Eur. Ass. Anim. Prod. 13, 125.Google Scholar
Waterlow, J. C., Garlick, P. J. & Millward, D. J. (1978). Protein Turnover in Mammalian Tissues. Ch. 17, 18. Amsterdam: Elsevier/Excerpta Medica/North Holland.Google Scholar